Auflösung von Amyloidaggregaten durch einen kontrolliert induzierten Übergang von einer β‐Faltblatt‐ in eine α‐Helix‐Struktur: eine Anwendung des Schalterkonzepts

Mimna, Richard; Camus, Marie‐Stéphanie; Schmid, Adrien W.; Tuchscherer, Gabriele; Lashuel, Hilal A.; Mutter, Manfred

doi:10.1002/ange.200603681

Cited by 20 publications

(8 citation statements)

References 34 publications

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“…[69] More recently, they designed a switch peptide that disrupts amyloid-like b-sheet assemblies by converting the peptides into a-helices. [70] Koksch et al synthesized peptide VW19 (LKVELKELK-KELVVLKSELKELKKEL) that contains structural elements matching both a-helical folding and b-sheet formation. Depending on the environmental conditions (pH and/or concentration of the peptide), it can assume a random-coil, bsheet, or coiled-coil conformation.…”

Section: Switch Peptidesmentioning

confidence: 99%

Smart Self‐Assembled Hybrid Hydrogel Biomaterials

2012

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Hybrid biomaterials are systems created from components of at least two distinct classes of molecules, for example, synthetic macromolecules and proteins or peptide domains. The synergistic combination of two types of structures may produce new materials that possess unprecedented levels of structural organization and novel properties. This Review focuses on biorecognition-driven self-assembly of hybrid macromolecules into functional hydrogel biomaterials. First, basic rules that govern the secondary structure of peptides are discussed, and then approaches to the specific design of hybrid systems with tailor-made properties are evaluated, followed by a discussion on the similarity of design principles of biomaterials and macromolecular therapeutics. Finally, the future of the field is briefly

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Section: Switch Peptidesmentioning

confidence: 99%

Smart Self‐Assembled Hybrid Hydrogel Biomaterials

2012

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“…Moreover, they can help to elucidate the molecular interactions that occur during structural transition and the formation of amyloid fibrils, and more importantly they can provide insights into different strategies for inhibiting amyloid formation. [41][42][43] We recently designed and synthesized a series of 26-residue model peptides that were based on the characteristic heptad repeat of the a-helical coiled-coil motif. By incorporating valine residues at three different solvent-exposed positions, the system was made more prone to amyloid formation.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Amyloid Aggregation by Formation of Helical Assemblies

Brandenburg

Berlepsch

Gerling

et al. 2011

Chemistry A European J

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The formation of amyloid aggregates is responsible for a wide range of diseases, including Alzheimer's and Parkinson's disease. Although the amyloid-forming proteins have different structures and sequences, all undergo a conformational change to form amyloid aggregates that have a characteristic cross-β-structure. The mechanistic details of this process are poorly understood, but different strategies for the development of inhibitors of amyloid formation have been proposed. In most cases, chemically diverse compounds bind to an elongated form of the protein in a β-strand conformation and thereby exert their therapeutic effect. However, this approach could favor the formation of prefibrillar oligomeric species, which are thought to be toxic. Herein, we report an alternative approach in which a helical coiled-coil-based inhibitor peptide has been designed to engage a coiled-coil-based amyloid-forming model peptide in a stable coiled-coil arrangement, thereby preventing rearrangement into a β-sheet conformation and the subsequent formation of amyloid-like fibrils. Moreover, we show that the helix-forming peptide is able to disassemble mature amyloid-like fibrils.

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“…For LC-MS, an analytical Vydac C4 column (Grace Vydac, 4.6 250 mm, 5 mm particle size, flow 1 mL min ) was employed, with the same buffer system as used for LC-MS. Milli-Q water with a resistance of more than 18.2 MW cm À1 was provided by a Millipore Milli-Q filtering system with filtration through a 0.22 mm Millipak filter. 1 H NMR and 13 C NMR spectra were measured with a Bruker AC-200 (200 and 50.1 MHz, respectively). Chemical shifts are reported in ppm downfield from internal tetramethylsilane (0.00 ppm).…”

Section: Experimental Section General Materials and Methodsmentioning

confidence: 99%

“…It has been shown that predefined transitions can be designed a priori, for instance, solution-to-gel, nematicto-isotropic phase, and random-coil-to-b-sheet transitions. [1] These findings have offered a way to generate discrete and smart nanostructures of b-sheet peptides, which is an important step in the production of functional materials. [2] Many scientists have studied the ability of b-sheet-forming amphiphilic peptides to self-assemble into several structures.…”

Section: Introductionmentioning

confidence: 98%

Assembly into β‐Sheet Structures upon Peptide–Liposome Conjugation through Copper(I)‐Catalyzed [3+2] Azide–Alkyne Cycloaddition

2014

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The random‐coil‐to‐β‐sheet transition of the (Leu‐Glu)4 peptide motif is induced upon its conjugation to the liposome surface through “click” chemistry. Circular dichroism (CD) spectroscopy enables the in situ monitoring of this reaction. A change in the peptide secondary structure is already observed within 15 min. The β‐sheet conformation becomes the dominant secondary structure after 45 min, as shown by the strong CD signal observed, which is typical for a β‐sheet peptide secondary structure.

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Auflösung von Amyloidaggregaten durch einen kontrolliert induzierten Übergang von einer β‐Faltblatt‐ in eine α‐Helix‐Struktur: eine Anwendung des Schalterkonzepts

Cited by 20 publications

References 34 publications

Smart Self‐Assembled Hybrid Hydrogel Biomaterials

Smart Self‐Assembled Hybrid Hydrogel Biomaterials

Inhibition of Amyloid Aggregation by Formation of Helical Assemblies

Assembly into β‐Sheet Structures upon Peptide–Liposome Conjugation through Copper(I)‐Catalyzed [3+2] Azide–Alkyne Cycloaddition

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